Evidence map›Paper›PMID 19578543›Full record

ArticlePloS one2009

Interactions between beta subunits of the KCNMB family and Slo3: beta4 selectively modulates Slo3 expression and function.

Cheng-Tao Yang, Xu-Hui Zeng, Xiao-Ming Xia, Christopher J Lingle

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 19% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

26 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. SLO3: A Conserved Regulator of Sperm Membrane Potential.International journal of molecular sciences · 2023
    Review
  5. Review
  6. A selective inhibitor of the sperm-specific potassium channel SLO3 impairs human sperm function.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. BK Channels in the Central Nervous System.International review of neurobiology · 2016
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Cheng-Tao YangDepartment of Anesthesiology, Washington University School of Medicine, St Louis, MO, USA.
Xu-Hui Zeng
Xiao-Ming Xia
Christopher J Lingle
Washington University in St. Louis · US

Funding

AUXILIARY SUBUNITS OF CA2+ ACTIVATED K+ CHANNELSR01GM081748 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2008 to 2015
$3.2M
Redox Regulation of Auxillary B subunits of BK ChannelsR01GM068580 · NIGMS · WASHINGTON UNIVERSITY · PI LINGLE, CHRISTOPHER J · 2003 to 2006
$1.2M
NIGMS NIH HHS GM068580NIGMS NIH HHS GM081748NIGMS NIH HHS R01 GM068580NIGMS NIH HHS R01 GM081748
6 · The paper itself

Abstract

backgroundThe pH and voltage-regulated Slo3 K(+) channel, a homologue of the Ca(2+)- and voltage-regulated Slo1 K(+) channel, is thought to be primarily expressed in sperm, but the properties of Slo3 studied in heterologous systems differ somewhat from the native sperm KSper pH-regulated current. There is the possibility that critical partners that regulate Slo3 function remain unidentified. The extensive amino acid identity between Slo3 and Slo1 suggests that auxiliary beta subunits regulating Slo1 channels might coassemble with and modulate Slo3 channels. Four distinct beta subunits composing the KCNMB family are known to regulate the function and expression of Slo1 Channels. METHODOLOGY/PRINCIPAL

findingsTo examine the ability of the KCNMB family of auxiliary beta subunits to regulate Slo3 function, we co-expressed Slo3 and each beta subunit in heterologous expression systems and investigated the functional consequences by electrophysiological and biochemical analyses. The beta4 subunit produced an 8-10 fold enhancement of Slo3 current expression in Xenopus oocytes and a similar enhancement of Slo3 surface expression as monitored by YFP-tagged Slo3 or biotin labeled Slo3. Neither beta1, beta2, nor beta3 mimicked the ability of beta4 to increase surface expression, although biochemical tests suggested that all four beta subunits are competent to coassemble with Slo3. Fluorescence microscopy from beta4 KO mice, in which an eGFP tag replaced the deleted exon, revealed that beta4 gene promoter is active in spermatocytes. Furthermore, quantitative RT-PCR demonstrated that beta4 and Slo3 exhibit comparable mRNA abundance in both testes and sperm. CONCLUSIONS/SIGNIFICANCE: These results argue that, for native mouse Slo3 channels, the beta4 subunit must be considered as a potential interaction partner and, furthermore, that KCNMB subunits may have functions unrelated to regulation of the Slo1 alpha subunit.

Indexed as

AnimalsBlotting, WesternCell LineHumansImmunoprecipitationLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMaleMiceNerve Tissue ProteinsReverse Transcriptase Polymerase Chain ReactionSpermatogoniaXenopus laevisKCNMB4 protein, humanKcnmb4 protein, mouseKcnu1 protein, mouseLarge-Conductance Calcium-Activated Potassium Channel beta SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsNerve Tissue Proteins

Identifiers

PMID19578543
PMCPMC2701609
OpenAlexW1972726121

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.